[Molecular diversities and functions of antibacterial peptides from the skins of Ranidae of amphibians.].
Granular glands in the frog skins of Ranidae of amphibians, a widely distributed group with over 650 species, synthesize and secrete a remarkably diverse array of peptides with the broad-spectrum antibacterial, antifungal and other biologic activities to protect the organism against a wide range of pathogens, which are believed to have arisen as a result of multiple gene duplication events. Almost without exception, these components are hydrophobic, cationic and form an amphipathic a-helix in a membrane-mimetic solvent. The peptides can be grouped into families on the basis of structural similarity. To date, brevinin-1, esculentin-1, esculentin-2, and temporin peptides, ranalexin, ranatuerin-1, ranatuerin-2 and palustrin, brevinin-2, tigerinin, japonicin, nigrocin and melittin-related peptides have been found in amphibians of Ranidae. In this paper, the molecular diversity, structural feature and the biological ac-tivity of Ranidae antibacterial peptides were reviewed.
Jin
Li-Li
LL
School of Life Science, Liaoning University, Shenyang 110036, China E-mail: lilijin@lnu.edu.cn.
Wang
Qiu-Yu
QY
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D008969:Molecular Sequence Data; D011898:Ranidae; D012867:Skin
D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents